Blickling S, Knäblein J
Max-Planck Institut für Biochemie, Martinsried, Germany.
Biol Chem. 1997 Mar-Apr;378(3-4):207-10. doi: 10.1515/bchm.1997.378.3-4.207.
Dihydrodipicolinate synthase (DHDPS) is the first enzyme unique to the lysine biosynthetic pathway and is feedback regulated by L-lysine in plants and some bacteria. The allosteric binding site has been localized by X-ray crystallography and is in agreement with reported mutations of plant DHDPS enzymes, which confer insensitivity to feedback inhibition. Three possible elements of the mechanism of lysine inhibition are discussed.
二氢吡啶二羧酸合酶(DHDPS)是赖氨酸生物合成途径中首个独特的酶,在植物和一些细菌中受L-赖氨酸的反馈调节。变构结合位点已通过X射线晶体学定位,并且与已报道的植物DHDPS酶突变相符,这些突变使酶对反馈抑制不敏感。本文讨论了赖氨酸抑制机制的三种可能因素。